Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q28C88

Entry ID Method Resolution Chain Position Source
AF-Q28C88-F1 Predicted AlphaFoldDB

No variants for Q28C88

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q28C88

1 associated diseases with Q28C88

[MIM: 116300]: Cataract 30, multiple types (CTRCT30)

An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549, ECO:0000269|PubMed:28450710}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549, ECO:0000269|PubMed:28450710}. Note=The disease is caused by variants affecting the gene represented in this entry.

3 regional properties for Q28C88

Type Name Position InterPro Accession
domain Intermediate filament head, DNA-binding domain 7 - 101 IPR006821
conserved_site Intermediate filament protein, conserved site 397 - 405 IPR018039
domain Intermediate filament, rod domain 102 - 411 IPR039008

Functions

Description
EC Number 2.3.1.22 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

1 GO annotations of molecular function

Name Definition
2-acylglycerol O-acyltransferase activity Catalysis of the reaction: acyl-CoA + 2-acylglycerol = CoA + diacylglycerol.

4 GO annotations of biological process

Name Definition
diacylglycerol biosynthetic process The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
glycerol metabolic process The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
triglyceride biosynthetic process The chemical reactions and pathways resulting in the formation of a triglyceride, any triester of glycerol.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q96PD7 DGAT2 Diacylglycerol O-acyltransferase 2 Homo sapiens (Human) PR
10 20 30 40 50 60
MKLEFAPINI PLARRLQTTA VFQWVFSFLL LAQCCIGIFL SLVLARLWLI LALYVLWLYL
70 80 90 100 110 120
DWETPQAGGR RWEWVRNWTV WKYFKDYFPI RLVKTCDLDP QHNYIMGFHP HGVLVAGAFG
130 140 150 160 170 180
NFCTNYTGFK ELFPGLTPYL HILPFWFRCP FFREYAMCVG LVSATKKSVN HVLSKENGGN
190 200 210 220 230 240
ISIIVIGGAE ESLDAHPGSL ILHILKRKGF IKVAFKQGAH LVPVFSFGEN ELFQQVPNPK
250 260 270 280 290 300
GSFLRCVQER LQKIMGFAMP LFHARGIFQY SFGLMPYRMP IHTVVGRPIP VKQTSHPTQE
310 320 330
EIESLHQQYL SALRDLFEEH KERYGIPEHE SLIFT